| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| Amplification of the M 2 gene encoding the small subunit of ribonucleotide reductase ( EC 1 . 17 . 4 . 1 ) was analyzed in a collection of vaccinia virus ( 10 ) isolates selected for resistance to 5 mM hydroxyurea ( HU ) . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| Two cDNAs , designated muAUF 1 3 and muAUF 1 7 , were isolated from a murine fetal cDNA library , using as a probe , a fragment of the p37AUF1 cDNA encoding RRM 1 and approximately half of RRM 2 . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| The isolated N terminal or C terminal RRM alone ( RRM 1 and RRM 2 , respectively ) is sufficient for binding nucleic acids with the binding specificity similar to that of the wild type RRM , although the binding affinity of the isolated RRM 2 is nearly two orders of magnitude lower than that of RRM 1 . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| Their behavioral significance was assayed by generating transgenic strains that were singly or multiply mutated within the relatively N terminal motif ( RRM 1 ) or within RRM 2 . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| Mapping of the ribonucleotide reductase genes ( Rrm 1 , Rrm 2 ) in the rat . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| The N terminal region of human hnRNP A 1 , termed unwinding protein 1 ( UP 1 ) , contains two RNA recognition motifs ( RRMs ) , RRM 1 and RRM 2 . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| Surprisingly , RRM 2 but not RRM 1 could support this function when duplicated , despite their very similar structure . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| As previously shown for yeast , human eIF4G binds to a fragment composed of RRM 1 and RRM 2 of PABP . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| Conjugation of the eight amino acid residues to RRM 1 enhanced the RNA binding as well as the entire RRM 2 , indicating that the octapeptide of RRM 2 can be compensated for by the binding function of RRM 2 . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| In the crystal structure , a UP 1 dimer binds to two strands of DNA , and each strand contacts RRM 1 of one monomer and RRM 2 of the other . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| The individual RRMs bind poorly to the RNA ( RRM 1 binds with micromolar affinity , while the affinities of RRM 2 and 3 are in the millimolar range ) . ^^^ However , the combination of RRM 1 and either RRM 2 or RRM 3 in the context of the protein allows binding with a nanomolar affinity . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| This analysis revealed that RRM 3 replacements were fully functional , but RRM 1 and RRM 2 replacements were largely nonfunctional . ^^^ Under less stringent conditions RRM 1 and RRM 2 replacements from SXL and RRM 1 replacement from RBP 9 were able to provide supplemental function in the presence of a mutant hypomorphic ELAV protein . . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| PSF comprises an N terminal proline and glutamine rich domain , two RRMs ( RRM 1 and RRM 2 ) , and a C terminal region that contains two nuclear localization signals , both of which are required for complete nuclear localization . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| The modular protein harbors a N terminal RNA recognition motif ( RRM ) , RRM 1 , and in the C terminal domain , a second , atypical RRM 2 , in addition to a phosphorylation site , and a putative nucleotide binding site . ^^^ The atypical RRM 2 in the C terminal domain of La has an unprecedented negative effect on 3 ' end RNA recognition , as indicated by a higher K ( d ) value of 90 + / 10 nm for the La RRM 1 RRM2 mutant but comparable specificity . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| RRM 1 and RRM 2 are essential for viability , although interestingly either domain can suffice for this function . ^^^ Finally , we show that mutations in RRM 1 , RRM 2 , or the RTZF do not affect the circadian regulation of eclosion , and we discuss possible interpretations of these results . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| Point mutations in RRM 1 or RRM 2 decreased the Kd for apo B mRNA by two orders of magnitude whereas mutations in RRM 3 reduced binding affinity 13 fold . ^^^ The pairwise expression of RRM 1 with RRM 2 or RRM 3 resulted in moderate affinity binding . . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| Human RNA binding protein HuR , a nucleocytoplasmic shuttling protein , is a ubiquitously expressed member of the family of Hu proteins , which consist of two N terminal RNA recognition motifs ( RRM 1 and RRM 2 ) , a hinge region , and a C terminal RRM ( RRM 3 ) . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| For both proteins , RRM 1 and RRM 2 together constitute the minimal Py tract recognition domain . ^^^ Both RRM 1 and RRM 2 of U2AF ( 65 ) and SXL can be cross linked to certain residues , with RRM 2 showing a surprisingly high number of residues cross linked . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| Using these methods , we quantified mRNA expression levels of deoxycytidine kinase ( dCK ) , deoxycytidylate deaminase ( dCDA ) , the M 1 and M 2 subunits of ribonucleotide reductase ( RRM 1 , RRM 2 ) , and excision cross complementation group 1 ( ERCC 1 ) in 35 human `` fresh ' ' frozen breast cancer biopsies . ^^^ This reproducible , highly sensitive real time RT PCR method for the detection and quantification of the mRNAs for dCK , dCDA , RRM 1 , RRM 2 , and ERCC 1 in human breast cancer biopsies appears to be more informative and less time consuming than either classical radioisotope dependent RT PCR or the technique utilizing GeneScan analysis described herein . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| CELF proteins contain two adjacent RNA binding domains ( RRM 1 and RRM 2 ) near the N terminus and one RRM ( RRM 3 ) near the C terminus , which are separated by a 160 230 residue divergent domain of unknown function . ^^^ Either RRM 1 or RRM 2 of CELF 4 are necessary and sufficient for binding MSE RNA and RRM 2 plus an additional 66 amino acids of the divergent domain are as effective as full length protein in activating MSE dependent splicing in vivo . ^^^ Non overlapping N and C terminal regions of ETR 3 containing either RRM 1 and RRM 2 or RRM 3 plus segments of the adjacent divergent domain activate MSE dependent exon inclusion demonstrating an unusual functional redundancy of the N and C termini of the protein . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| RNA was extracted from tumor and normal lung tissue , and expression of the genes RRM 1 , PTEN , and RRM 2 was determined by real time quantitative polymerase chain reaction . ^^^ RESULTS : RRM 1 expression was significantly correlated with PTEN and RRM 2 expression in tumor tissue . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| A partial revertant of H 358 G200 cells had reduced levels of RRM 1 protein ( compared with G 200 cells ) , without observed changes in RRM 2 or p53R2 . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NMR structural analysis of the N terminal half of PTB ( residues 55 301 ) shows a canonical structure for RRM 1 but reveals novel extensions to the beta strands and C terminus of RRM 2 that significantly modify the beta sheet RNA binding surface . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| A newly identified temperature sensitive lethal point mutation in RRM 1 is exacerbated by mutations in the U 6 RNA telestem , as is a mutation in RRM 2 , but not one in RRM 3 . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| The role of drug transport and metabolism on gemcitabine cytotoxicity was examined with specific inhibitors , whereas transcription analysis of human equilibrative nucleoside transporter 1 ( hENT 1 ) , deoxycytidine kinase ( dCK ) , 5 ' nucleotidase ( 5 ' NT ) , cytidine deaminase ( CDA ) , and ribonucleotide reductase subunits M 1 and M 2 ( RRM 1 and RRM 2 ) was done by quantitative reverse transcription PCR in tumor tissue isolated by laser microdissection from surgical or biopsy samples of 102 patients . ^^^ Transport and metabolism had a key role on gemcitabine sensitivity in vitro ; moreover , hENT 1 , dCK , 5 ' NT , CDA , RRM 1 , and RRM 2 were detectable in most tumor specimens . hENT 1 expression was significantly correlated with clinical outcome . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| RRM 1 is not able to bind RNA by itself in vitro , but a construct combining RRM 1 with a newly identified downstream RRM 2 specifically binds RNA . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| The nucleotide metabolism enzyme ribonucleotide reductase is composed of a regulatory subunit ( RRM 1 ) and a catalytic subunit ( RRM 2 ) . ^^^ |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P23921 and P31350 |
Pubmed |
SVM Score :0.0 |
| NA |
|